DocumentCode :
3607673
Title :
Catalytic role of traditional enzymes for biosynthesis of biogenic metallic nanoparticles: a mini-review
Author :
Dura?Œ??n, Marcela ; Silveira, Camila P. ; Dura?Œ??n, Nelson
Author_Institution :
Biol. Chem. Lab., Univ. Estadual de Campinas, Campinas, Brazil
Volume :
9
Issue :
5
fYear :
2015
Firstpage :
314
Lastpage :
323
Abstract :
Although the formation mechanism of biogenically metallic nanoparticles is broadly associated to enzyme mediation, major attention has been given to the role of proteins and peptides in oxido-reduction of metallic ions leading to these nanostructures. Among the wide range of biomolecules that can act not only as capping agents but also as non-enzymatic agents to form nanoparticles, disulphide bridge-containing peptides and amino acids particularly stand out. The literature proposes that they actively participate in the process of nanoparticles´ synthesis, with thiols groups and disulphide bridge moieties as the reaction catalytic sites. Similarly, denaturated enzymes containing exposed S-S or S-H moieties are also able to reduce metallic ions to form nanoparticles. This mini-review is focused on the biogenic synthesis of metallic nanoparticles such as gold, silver, copper, platinum, palladium, lead and selenium, in which proteins, peptides, reductases and even oxido-reductases act as non-enzymatic catalysts of the reduction reaction, opening economically and ecologically favourable perspectives in the nanoparticles synthesis field.
Keywords :
catalysis; copper; enzymes; gold; lead; molecular biophysics; nanobiotechnology; nanoparticles; oxidation; palladium; platinum; reduction (chemical); selenium; silver; Ag; Au; Cu; Pb; Pd; Pt; Se; amino acids; biogenic metallic nanoparticles; biomolecules; biosynthesis; copper; disulphide bridge; enzymes; gold; lead; nonenzymatic catalysts; oxido-reductases; oxido-reduction; palladium; peptides; platinum; proteins; reduction reaction; selenium; silver;
fLanguage :
English
Journal_Title :
Nanobiotechnology, IET
Publisher :
iet
ISSN :
1751-8741
Type :
jour
DOI :
10.1049/iet-nbt.2014.0054
Filename :
7289525
Link To Document :
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